Method for endotoxin removal
    39.
    发明授权
    Method for endotoxin removal 有权
    内毒素去除方法

    公开(公告)号:US09580692B2

    公开(公告)日:2017-02-28

    申请号:US14380477

    申请日:2013-02-27

    Abstract: The present invention relates to a method for endotoxin removal from a sample comprising the following steps: combining the sample comprising one or more target molecule(s) with a chromatography media comprising beads having an inner porous core functionalized with ligands capable of binding endotoxin and an outer porous layer without functional groups and a pore size small enough to exclude the target molecule from the inner core; and collecting the sample from the media, wherein the sample comprises an endotoxin level which is at least 75% less, preferably 90% less, than before the removal and the yield of the target molecule is at least 75%.

    Abstract translation: 本发明涉及一种从样品中去除内毒素的方法,包括以下步骤:将包含一种或多种靶分子的样品与包含珠的色谱介质组合,所述珠粒具有由能够结合内毒素的配体功能化的内部多孔核心和 没有官能团的外部多孔层和足够小以从靶芯排出靶分子的孔径; 并从培养基中收集样品,其中样品包含与去除前相比至少75%以上,优选90%以下的内毒素水平,并且目标分子的产率为至少75%。

    Method of Storing a Separation Matrix
    40.
    发明申请

    公开(公告)号:US20200239517A1

    公开(公告)日:2020-07-30

    申请号:US16095721

    申请日:2017-05-10

    Abstract: The present invention concerns a method of storing a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains covalently coupled to a porous support. The method comprises the steps of: a) providing a storage liquid comprising at least 50% by volume of an aqueous alkali metal hydroxide solution; b) permeating the separation matrix with the storage liquid; and c) storing the storage liquid-permeated separation matrix for a storage time of at least days. The alkali-stabilized Protein A domains comprise mutants of a parental Fc-binding domain of Staphylococcus Protein A (SpA), as defined by, or having at least 80% such as at least 90%, 95% or 98% identity to, SEQ ID NO 51 or SEQ ID NO 52, wherein the amino acid residues at positions 13 and 44 of SEQ ID NO 51 or 52 are asparagines and wherein at least the asparagine residue at position 3 of SEQ ID NO 51 or 52 has been mutated to an amino acid selected from the group consisting of glutamic acid, lysine, tyrosine, threonine, phenylalanine, leucine, isoleucine, tryptophan, methionine, valine, alanine, histidine and arginine.

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